› 1uwy

X-ray diffraction
3Å resolution

Crystal structure of human carboxypeptidase M

Released:
DOI: 10.2210/pdb1uwy/pdb
PDB entry 1uwy coloured by chain, front view.
PDB entry 1uwy coloured by chain, side view.
PDB entry 1uwy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
Reverter D, Maskos K, Tan F, Skidgel RA, Bode W
J Mol Biol 338 257-69 (2004)
PMID: 15066430

Function and Biology Details

Reaction catalysed: 
Cleavage of C-terminal arginine or lysine residues from polypeptides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146936 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Carboxypeptidase M Chain: A
Molecule details ›
Chain: A
Length: 426 amino acids
Theoretical weight: 48.72 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P14384 (Residues: 18-443; Coverage: 100%)
Gene name: CPM
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P3221
Unit cell:
a: 85.83Å b: 85.83Å c: 124.54Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.286
Expression system: Spodoptera frugiperda

Quick links

Citations

9 review citations

Differential regulation of inducible and endothelial nitric oxide synthase by kinin B1 and B2 receptors.
Kuhr et al. (2010)
8 more

5 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
4 more